An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems
AUTOR(ES)
Gómez, GN, Nerli, BB, Acosta, OC, Picó, GA, Leiva, LCA
FONTE
J. Venom. Anim. Toxins incl. Trop. Dis
DATA DE PUBLICAÇÃO
2012
RESUMO
Snake venoms are rich sources of active proteins that have been employed in the diagnosis and treatment of health disorders and antivenom therapy. Developing countries demand fast economical downstream processes for the purification of this biomolecule type without requiring sophisticated equipment. We developed an alternative, simple and easy to scale-up method, able to purify simultaneously protease and phospholipase A2 toxins from Bothrops alternatus venom. It comprises a multiple-step partition procedure with polyethylene-glycol/phosphate aqueous two-phase systems followed by a gel filtration chromatographic step. Two single bands in SDS-polyacrylamide gel electrophoresis and increased proteolytic and phospholipase A2 specific activities evidence the homogeneity of the isolated proteins.
Documentos Relacionados
- Two-phase aqueous micellar systems: an alternative method for protein purification
- A SOLVATION-BASED THERMODYNAMIC MODEL FOR AQUEOUS TWO-PHASE SYSTEMS
- Separation of organic dust from microorganism suspensions by partitioning in aqueous polymer two-phase systems.
- New Insights into the Partitioning of Phenothiazine Dyes in Aqueous Two-Phase Systems
- Selective partitioning of conidia of some Penicillium and Aspergillus species in aqueous two-phase systems.